Modulation of the Disordered Conformational Ensembles of the p53 Transactivation Domain by Cancer-Associated Mutations
Fig 4
A) Comparison of the average residue helicity profile with the secondary Hα chemical shifts for the wild-type p53-TAD[38].
The uncertainties of the average residue helicities were estimated as the difference between values calculated from the folding and control RE-GA runs (see Fig 2A). The reference random coil values were taken from statistics of the BMRB database[50]. B) Back-calculated RDC profiles in comparison with the experimental one[39]. Note that the calculated profiles were globally scaled to best reproduce the experimental values.